ELECTRON-MICROSCOPIC LOCALIZATION OF HYDROLYTIC ENZYMES IN OSTEOCLASTS
ELECTRON-MICROSCOPIC LOCALIZATION OF HYDROLYTIC ENZYMES IN OSTEOCLASTS
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DOI：
10.1007/bf01890996
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发表时间：
1972-01-01
期刊：
影响因子：
--
通讯作者：
SCHOFIELD, BH
中科院分区：
文献类型：
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作者：
DOTY, SB;SCHOFIELD, BH
酸性甘油磷酸酶的活性（最适pH值，5.0）已被发现破骨细胞内的许多工人，但相对较少的研究一直关注的中性水解酶的pH值约为7.2。本文证明了对硝基苯磷酸盐、ATP和对氯苯胺膦酸盐都能表现出中性酶活性。对β-甘油磷酸盐、无机三偏磷酸盐或p-硝基儿茶酚硫酸盐作为底物的活性被发现限于酸性pH范围。电子显微镜证据表明，许多水解酶存在于破骨细胞的单个膜结合体、空泡、高尔基体和无颗粒内质网中。这种网状物扩张形成大的溶酶体。这种活动是distingingly不同的功能高尔基膜在其形成的初级lysosome.The溶酶体，细胞质空泡，和细胞外释放的酶通过专门的'皱褶'边界之间的关系显示和讨论。
Acid glycerophosphatase activity (pH optimum, 5.0) has been found within osteoclasts by numerous workers but relatively few studies have been concerned with the neutral hydrolytic enzymes that have pH optima around 7.2. Evidence is presented in this paper to show that neutral enzyme activity can be demonstrated withp-nitrophenyl phosphate, ATP andp-chloranilidophosphonate as substrates. Activity against β-glycerophosphate, inorganic trimetaphosphate orp-nitrocatachol sulphate as substrates was found to be limited to an acid pH range.Electron microscopic evidence indicated that many of the hydrolytic enzymes were present within single membrane-bound bodies, vacuoles, Golgi elements, and the agranular endoplasmic reticulum of the osteoclast. This reticulum was dilated to form large lysosomes. Such activity was distingly different from the function of the Golgi membrane in its formation of primary lysosomes.The relationships between lysosomes, cytoplasmic vacuoles, and extracellular release of enzyme through the specialized ‘ruffled’ border are shown and discussed.